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Biomedical subjects

M Rolland

Publications and source records attributed to M Rolland.

At least 91 records · Page 5Linked to original sources
PubMed1982

[Haemorrhages of the posterior fossa in full-term newborns (author's transl)].

Four cases of non-traumatic haemorrhage of the posterior fossa in full-term newborns are reported and compared with the 30 cases already published. Computerized tomography is the only method that permits both a diagnostic and a therapeutic approach. Surgery is indicated in the presence of brain stem compression but should be carefully discussed in cases of intracerebellar haemorrhage with secondary extension to the posterior fossa. Early hydrocephalus is common and requires shunting in about 25% of the cases

Cerebellar Diseases↗
PubMed1982

Structure-function relationship in thyroglobulin: amino acid sequence of two different thyroxine-containing peptides from porcine thyroglobulin.

From the cyanogen bromide (CNBr) treatment of porcine thyroglobulin a peptide of mol. wt. 15 000, CNBr-b1, was purified by gel filtration and ion-exchange chromatography. CNBr-b1 contained 50% of the thyroxine (T4) content of the protein. After digestion with trypsin and protease from Staphylococcus aureus V-8, thyroxine-containing peptides were purified and analyzed by microsequence analysis using the colored Edman's reagent dimethylaminoazobenzeneisothiocyanate . Two different sequences harboring T4 were identified: sequence 1, His-Asp-Asp-Asp-T4-Ala-Thr-(Glx,Gly)-Leu-Tyr-Phe-Ser-Ser-Arg, which contains 1 mol T4/mol peptide and sequence 2, Asp-(Tyr/MIT/DIT/T4)-Phe-Ile-Leu-X-Pro-Val-, which is a mixture of the same peptide at different levels of iodination and coupling. These sequences are likely to be representative of distinct hormonogenic sites, the former giving evidence of early iodinated tyrosine residues where preferential coupling into hormonal residues occurs especially at low iodine levels and the latter representing less reactive site(s) operative at higher iodine levels.

Amino Acid Sequence↗
PubMed1982

[Idiopathic thrombopenic purpura and pregnancy].

The association of IPT (idiopathic thrombocytopenic purpura) and pregnancy happens rarely, but when it does it gives rise to two problems, the maternal and the neonatal. On the maternal level the risk is haemorrhage. Furthermore, the role of splenectomy in pregnancy still needs to be discussed; whereas all authors agree that treatment with corticoids and perhaps even with platelet transfusion may be necessary. As far as the newborn are concerned, it is common to find a low level of platelets which means that the newborn has particular risks of blood vessel rupture and intra-cranial haemorrhage (our observation). The attitude that the authors propose as far as the obstetric management of these cases is concerned is to carry out routine Caesarean section at term before labour starts. They analyse the other methods of dealing with these cases from the point of view of the maternal platelets and also from the fetal platelets estimated from scalp blood during labour.

Adult↗
PubMed1980

An approach to the structure of thyroglobulin. Hormone-forming sequences in porcine thyroglobulin.

The mixture of CNBr peptides obtained by treatment of porcine thyroglobulin with cyanogen bromide was separated into three fractions by Sephadex G-200 gel filtration in 1 M propionic acid. When one of these fractions was reduced and S-alkylated, a hormone-containing CNBr peptide was purified by filtration on Biogel A-1.5 m and ion-exchange chromatography on DEAE-Sephadex. Similarly, two other hormone-containing CNBr peptides were separated from another reduced and S-alkylated fraction by Sephacryl S-200 gel filtration and DEAE-Sephadex chromatography. The three purified CNBr peptides have the same Mr (15000), differ in amino acid composition and contain 60-70% of the hormones present in the initial thyroglobulin. Fragmentation of these peptides into smaller hormone peptides was carried out by trypsin digestion followed by gel filtration. This resulted in the purification of eight discrete hormone-containing tryptic peptides whose homogeneity was established by the study of their N-terminal and C-terminal sequences. At least four sites for the synthesis of thyroxine and two sites for the synthesis of triiodothyronine have been identified in the three CNBr peptides. A possible additional site was recovered in the form of the peptides seryl-triiodothyronine and probably seryl-thyroxine. To gain information on the number of hormone-forming sites in thyroglobulin iodinated in vivo and on the distribution of these sites in the different hormone-containing peptides isolated, estimation of thyroxine and triiodothyronine content of batches of thyroglobulin of iodine content comprised between 0.73% and 1.6% was carried out, together with the estimation of the hormone content of all the CNBr peptides separated from two preparations of thyroglobulin of different iodine contents (0.73% and 1.23%). It was shown that the number of thyroxine and triiodothyronine residues increased linearly with increasing thyroglobulin iodine content in the range 0.73-1.6% and reached six residues of thyroxine and two residues of triiodothyronine/mol protein for a thyroglobulin iodine content of 1.6% with no indication of saturation. This result is at variance with previous findings on porcine thyroglobulin iodinated in vivo which suggested that the thyroxine content reached a plateau of three to four residues/molecule for an iodine content comprised between 0.7% and 1.1%.

Amino Acid Sequence↗
PubMed1980

[Neonatal intestinal obstruction due to congenital hypothyroidism (author's transl)].

Three children with subacute neonatal intestinal obstruction are described in whom the diagnosis of congenital megacolon was suspected. The radiological changes improved when oral feeding stopped but reappeared when it was restarted. The aetiology remained unrecognised until the results of the neonatal screening for hypothyroidism showed all three cases had congenital hypothyroidism. The severity of the disorders was unusual and remains unexplained. Systemic TSH and/or T4 determinations should lead to a better understanding of the disorders due to hyperthyroidism in neonates.

Congenital Hypothyroidism↗
PubMed1977

Polypeptide chains of 19-S thyroglobulin from several mammalian species and of porcine 27-S iodoprotein.

Undegraded 19-S thyroglobulin was purified from hog, ox, man, dog, sheep and rat thyroid glands. Sodium dodecylsulfate/ polyacrylamide gel electrophoresis of the reduced proteins showed that all are formed of peptide chains of molecular weight about 330000. Carboxypeptidase A digestion of porcine 19-S thyroglobulin released consecutively two moles of leucine and then two moles of serine, thus offering strong evidence in favour of the idea that the protein is formed of two identical chains. The same C-terminal amino acids were detected in sheep, ox, dog and man thyroglobulins. No N-terminal amino acid was found by appropriate chemical and enzymatic techniques. Porcine 27-S iodoprotein was shown by carboxypeptidase A analysis to be formed of four single-stranded 330000-Mr subunits identical to those constituting the 19-S protein. Identity, both qualitatively and quantitatively, of the peptides obtained by CNBr cleavage of the two proteins as shown by sodium dodecylsulfate/polyacrylamide gel electrophoresis has confirmed this conclusion. Since 19-S and 27-S thyroid iodoproteins are formed of two and four probably identical chains, they must be termed 19-S and 27-S thyroglobulins or alternatively thyroglobulin dimer and tetramer, respectively.

Amino Acids↗
PubMed1977

[Partial trisomy 10p of paternal origin. 2 new cases in 2 different families].

Two unrelated patients with partial trisomy 10p due to a paternal balanced translocation are reported. Though the sizes of the trisomic segment are not identical, both patients show: severe growth retardation, important psychomotor retardation and a dysmorphic mouth recalling a "tortois mouth". These observations are compared to twelve others from the literature.

Abnormalities, Multiple↗
PubMed1977

[Clouston's ectodermal dysplasia. A case report with biochemical study of keratin].

One familial case of ectodermal dysplasia of the Clouston's type is reported. The clinical picture consisted of hypotrichosis and dysonychia with normal sweating. The disease follows dominant autosomal transmission. Histologically, keratin was slightly abnormal. The biochemical study of keratin of hair and nails showed diminished cysteine.

Child↗
PubMed1976

Leukocyte cytochemical reactions in preterm and small for date babies.

Four cytochemical reactions widely used for hematological diagnosis (Myeloperoxydase, leukocyte alkaline phosphatase, PAS and Sudan Black) were carried out in 46 infants admitted into a neonatology unit (14 preterm babies, 19 small for date newborn infants (SDB) and 13 preterm with retarded intra-uterine growth). The MPO, polymorphonuclear PAS and Sudan Black levels are comparable in the three groups of infants and the same as in normal full-term newborn babies. On the other hand, the LAP level, identical in preterms and SDB, is lower than in full-term infants but higher than in adults. Lymphocyte PAS value increases progressively with age. Better interpretation of results would be gained with knowledge of normal ranges for these four parameters in children. The authors suggest that these reactions should be used in the field of general metabolic diseases, susceptibility to infection and genetic diseases with or without chromosal abnomaly.

Alkaline Phosphatase↗
PubMed1976

Endogenous proteolytic activity and constituent polypeptide chains of sheep and pig 19 S thyroglobulin.

Porcine and ovine 19-S thyroglobulins prepared from frozen glands in several buffers using slice extraction or homogenization, ammonium sulfate precipitation and DEAE-cellulose chromatography or Sepharose 6B gel filtration were contaminated with protease activity of pH optima 4.5 and 8.6, as shown by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Optimum temperatures of autodigestion were 37 degrees C at pH 4.5 and 25 degrees C at pH 8.6. Thyroglobulins prepared from unfrozen glands pH 7.2 in 0.1 M sodium phosphate using slice extraction, ammonium sulfate precipitation and Sepharose 6B gel filtration were devoid of acid proteolytic activity but still underwent autodigestion at pH 8.6. Diisopropylfluorophosphate was a potent inhibitor of the alkaline protease activity of ovine thyroglobulin preparations. In contrast to thyroglobulin obtained from frozen glands the proteins purified from fresh unfrozen glands at pH 7.2 only showed the 19-S and the 12-S species by electrophoresis in sodium dodecyl sulfate polyacrylamide gels. Very few bands migrating faster than 12-S were visible. After full reduction and S-alkylation of porcine and ovine thyroglobulins, no qualitative changes were observed in the gel electrophoresis pattern as compared to the unmodified proteins. Species of apparent mol. wt. corresponding to the native 12 S were the major component, strongly suggesting a mol. wt. of about 330 000 for the elementary peptide chains of pig and sheep thyroglobulins.

Animals↗